Injuries related to hiking with a pack during National Outdoor Leadership School courses: a risk factor analysis.

OBJECTIVES: To determine if packweight, anthropometry, and individual characteristics are related to acute musculoskeletal and soft tissue injuries while wearing backpacks on wilderness expeditions. METHODS: This was a review of prospectively gathered data on participants and instructors enrolled in National Outdoor Leadership School Rocky Mountain hiking courses between March 2008 and October 2009. Packweight, height, body weight, age, and gender were collected. Individuals that suffered acute musculoskeletal and soft tissue injuries while hiking with a backpack were recorded and compared to individuals that did not suffer injuries. Logistic regression was used to determine which variables were significantly correlated with injuries. Odds ratios with associated confidence intervals and p-values are reported. RESULTS: One thousand two hundred and one individuals were included in the final analysis. Twenty-six individuals of this population suffered reportable musculoskeletal and soft tissue injuries while hiking with a pack. None of the factors examined (packweight, height, body weight, age, gender, or packweight to body weight ratio) were significant in predicting acute injury. CONCLUSIONS: Based on our results, an individual's packweight, anthropometry, and individual characteristics neither increase nor decrease their risk of experiencing a musculoskeletal or soft tissue injury while hiking with a backpack. Other factors, including fitness, pretrip training, and footwear, should be examined to determine appropriate strategies to reduce significant musculoskeletal and soft tissue injuries on wilderness expeditions.

Identification of human mannose binding lectin (MBL) recognition sites for novel inhibitory antibodies.

Mannose binding lectin (MBL) binding initiates activation of the lectin complement pathway. Recent studies from our laboratory have demonstrated that MBL-dependent complement activation mediates cellular injury following oxidative stress in vivo and in vitro. A panel of novel inhibitory monoclonal antibodies (MAbs) against MBL (e.g., MAb 3F8, 2A9, and hMBL1.2) has been developed that inhibit MBL binding and lectin pathway activation. Here, we further characterized the interactions of these MAbs and their Fab fragments to MBL. Whole MAbs or their Fab fragments bound to MBL with relatively high affinity. Fab fragments of 3F8 were functionally effective in inhibiting MBL-dependent complement activation, however, steric hindrance of MAb 2A9 was essential for inhibition of MBL-dependent complement activation. We identified the hinge region, and residues EDCVLLL within the carbohydrate recognition domain of MBL as the recognition sites for MAb 3F8 and 2A9, respectively. The interaction of MAbs (e.g., 3F8 and 2A9) to MBL was dependent on the conformation of their recognition sites. These findings demonstrate that MBL binding can be inhibited by at least two separate and independent mechanisms.